Cadherins are calcium-dependent homophilic cell adhesion
proteins essential for tissue organization. Establishment of stable cell-cell adhesion
depends on association of classical Cadherins with
Catenins, which links cell surface adhesion and recognition
to both Actincytoskeleton and
cell signaling pathways. Catenin (cadherin-associated protein), beta 1
(Beta-catenin) binds with high affinity to the distal
Cadherin cytoplasmic tail and, in turn, recruits Catenin
(cadherin-associated protein), alpha 1, 102kDa
(Alpha-catenin) to the complex.
Alpha-catenin binds to Actin
filaments directly and can also associate with a range of other actin-binding proteins
such as Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 4
(AF-6) and Formin. In contrast,
Catenin delta 1(p120-catenin)
binds directly to Cadherin independently of the other
catenins. Cadherin-Catenins
complex can further interact with a range of signaling molecules which participate in
either cellular signaling or control of cytoskeletal dynamics [1]. Stability
of the Cadherin/ Catenins
complex and thereby the integrity of adherent junction is controlled by phosphorylation/
dephosphorylation. Phosphorylation of Beta-catenin by
receptor- and non-receptor-types tyrosine kinases results in dissociation of
Alpha-catenin from Beta-catenin
with concomitant loss of cadherin adhesion, whereas tyrosine phosphatases ensure or
restore the integrity of Cadherin-mediated adhesions [2].

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